Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
2016
Autori
Apostolović, DanijelaStanić-Vučinić, Dragana
de Jongh, Harmen H. J.
de Jong, Govardus A. H.
Mihailović-Vesić, Jelena
Radosavljević, Jelena
Radibratović, Milica
Nordlee, Julie A.
Baumert, Joseph L.
Milčić, Miloš K.
Taylor, Steve L.
Clua, Nuria Garrido
Ćirković-Veličković, Tanja
Koppelman, Stef J.
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune s...ystem, providing an explanation for the extraordinary allergenicity of peanut conglutins.
Izvor:
Scientific Reports, 2016, 6Izdavač:
- Nature Publishing Group, London
Finansiranje / projekti:
- Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (RS-172024)
- Modeliranje i numeričke simulacije složenih višečestičnih sistema (RS-171017)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
Napomena:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3415
DOI: 10.1038/srep29249
ISSN: 2045-2322
PubMed: 27377129
WoS: 000379265400001
Scopus: 2-s2.0-84977267167
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Apostolović, Danijela AU - Stanić-Vučinić, Dragana AU - de Jongh, Harmen H. J. AU - de Jong, Govardus A. H. AU - Mihailović-Vesić, Jelena AU - Radosavljević, Jelena AU - Radibratović, Milica AU - Nordlee, Julie A. AU - Baumert, Joseph L. AU - Milčić, Miloš K. AU - Taylor, Steve L. AU - Clua, Nuria Garrido AU - Ćirković-Veličković, Tanja AU - Koppelman, Stef J. PY - 2016 UR - https://cherry.chem.bg.ac.rs/handle/123456789/2273 AB - Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins. PB - Nature Publishing Group, London T2 - Scientific Reports T1 - Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity VL - 6 DO - 10.1038/srep29249 ER -
@article{ author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.", year = "2016", abstract = "Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.", publisher = "Nature Publishing Group, London", journal = "Scientific Reports", title = "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity", volume = "6", doi = "10.1038/srep29249" }
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J.. (2016). Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports Nature Publishing Group, London., 6. https://doi.org/10.1038/srep29249
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports. 2016;6. doi:10.1038/srep29249 .
Apostolović, Danijela, Stanić-Vučinić, Dragana, de Jongh, Harmen H. J., de Jong, Govardus A. H., Mihailović-Vesić, Jelena, Radosavljević, Jelena, Radibratović, Milica, Nordlee, Julie A., Baumert, Joseph L., Milčić, Miloš K., Taylor, Steve L., Clua, Nuria Garrido, Ćirković-Veličković, Tanja, Koppelman, Stef J., "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity" in Scientific Reports, 6 (2016), https://doi.org/10.1038/srep29249 . .